A multiprotein complex mediates the ATP-dependent assembly of spliceosomal U snRNPs (original) (raw)
References
Will, C. L. & Luhrmann, R. Spliceosomal UsnRNP biogenesis, structure and function. Curr. Opin. Cell Biol.13, 290–301 (2001). ArticleCAS Google Scholar
Achsel, T. et al. A doughnut-shaped heteromer of human Sm-like proteins binds to the 3′-end of U6 snRNA, thereby facilitating U4/U6 duplex formation in vitro. EMBO J.18, 5789–5802 (1999). ArticleCAS Google Scholar
Seraphin, B. Sm and Sm-like proteins belong to a large family: identification of proteins of the U6 as well as the U1, U2, U4 and U5 snRNPs. EMBO J.14, 2089–2098 (1995). ArticleCAS Google Scholar
Zhang, D., Abovich, N. & Rosbash, M. A biochemical function for the Sm complex. Mol. Cell7, 319–329 (2001). ArticleCAS Google Scholar
Mattaj, I. W. & De Robertis, E. M. Nuclear segregation of U2 snRNA requires binding of specific snRNP proteins. Cell40, 111–118 (1985). ArticleCAS Google Scholar
Mattaj, I. W. in Structure and Function of Major and Minor Small Nuclear Ribonculeoprotein Particles (ed. Birnstiel, M.) 100–114 (Springer-Verlag, Berlin/NewYork, 1988). Book Google Scholar
Neuman de Vegvar, H. E. & Dahlberg, J. E. Nucleocytoplasmic transport and processing of small nuclear RNA precursors. Mol. Cell. Biol.10, 3365–3375 (1990). ArticleCAS Google Scholar
Fischer, U. & Luhrmann, R. An essential signaling role for the m3G cap in the transport of U1 snRNP to the nucleus. Science249, 786–790 (1990). ArticleCAS Google Scholar
Raker, V. A., Plessel, G. & Luhrmann, R. The snRNP core assembly pathway: identification of stable core protein heteromeric complexes and an snRNP subcore particle in vitro. EMBO J.15, 2256–2269 (1996). ArticleCAS Google Scholar
Raker, V. A., Hartmuth, K., Kastner, B. & Lührmann, R. Spliceosomal U snRNP core assembly: Sm proteins assemble onto a Sm site RNA nonanucleotide in a specific and thermodynamically stable manner. Mol. Cell. Biol.19, 6554–6565 (1999). ArticleCAS Google Scholar
Fischer, U., Liu, Q. & Dreyfuss, G. The SMN–SIP1 complex has an essential role in spliceosomal snRNP biogenesis. Cell90, 1023–1029 (1997). ArticleCAS Google Scholar
Buhler, D., Raker, V., Luhrmann, R. & Fischer, U. Essential role for the tudor domain of SMN in spliceosomal U snRNP assembly: implications for spinal muscular atrophy. Hum. Mol. Genet.8, 2351–2357 (1999). ArticleCAS Google Scholar
Liu, Q., Fischer, U., Wang, F. & Dreyfuss, G. The spinal muscular atrophy disease gene product, SMN, and its associated protein SIP1 are in a complex with spliceosomal snRNP proteins. Cell90, 1013–1021 (1997). ArticleCAS Google Scholar
Charroux, B. et al. Gemin3: a novel DEAD box protein that interacts with SMN, the spinal muscular atrophy gene product, and is a component of gems. J. Cell Biol.147, 1181–1194 (1999). ArticleCAS Google Scholar
Grundhoff, A. T. et al. Characterisation of DP103, a novel DEAD box protein that binds to the Epstein–Barr virus nuclear proteins EBNA2 and EBNA3C. J. Biol. Chem.27, 19136–19144 (1999). Article Google Scholar
Charroux, B. et al. Gemin4. A novel component of the SMN complex that is found in both gems and nucleoli. J. Cell Biol.148, 1177–1186 (2000). ArticleCAS Google Scholar
Meister, G. et al. Characterization of a nuclear 20S complex containing the survival of motor neurons (SMN) protein and a specific subset of spliceosomal Sm proteins. Hum. Mol. Genet.9, 1977–1986 (2000). ArticleCAS Google Scholar
Müller, B., Link, J. & Smythe, C. Assembly of U7 small nuclear ribonucleoprotein particle and histone RNA 3′ processing in Xenopus egg extracts. J. Biol. Chem.275, 24284–24293 (2000). Article Google Scholar
Jarmolowski, A. & Mattaj, I. W. The determinants for Sm protein binding to Xenopus U1 and U5 snRNAs are complex and non-identical. EMBO J.12, 223–232 (1993). ArticleCAS Google Scholar
Hunt, S. L., Hsuan, J. J., Totty, N. & Jackson, R. J. unr, a cellular cytoplasmic RNA-binding protein with five cold-shock domains, is required for internal initiation of translation of human rhinovirus RNA. Genes Dev.13, 347–448 (1998). Google Scholar
Johnson, J. L. & Craig, E. A. Protein folding in vivo: unraveling complex pathways. Cell90, 201–204 (1997). ArticleCAS Google Scholar
Pu, W. T., Krapivinsky, G. P., Krapivinsky, L. & Clapham, D. E. pICln inhibits snRNP biogenesis by binding core spliceosomal proteins. Mol. Cell. Biol.19, 4113–4120 (1999). ArticleCAS Google Scholar
Friesen, W. J., Massenet, S., Paushkin, S., Wyce, A. & Dreyfuss, G. SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets. Mol. Cell7, 1111–1117 (2001). ArticleCAS Google Scholar
Friesen, W. J. & Dreyfuss, G. Specific sequences of the Sm and Sm-like (Lsm) proteins mediate their interaction with the spinal muscular atrophy disease gene product (SMN). J. Biol. Chem.275, 26370–26375 (2000). ArticleCAS Google Scholar
Liu, Q. & Dreyfuss, G. A novel nuclear structure containing the survival of motor neurons protein. EMBO J.15, 3555–3565 (1996). ArticleCAS Google Scholar
Jones, K. W. et al. Direct interaction of the spinal muscular atrophy disease protein SMN with the core snoRNP protein fibrillarin. J. Biol. Chem. (in the press).
Pellizzoni, L., Baccon, J., Charroux, B. & Dreyfuss, G. The survival of motor neurons (SMN) protein interacts with the snoRNP proteins fibrillarin and GAR1. Curr. Biol.11, 1079–1088 (2001). ArticleCAS Google Scholar
Lerner, E. A., Lerner, M. R., Hardin, J. A., Janeway, C. A. & Steitz, J. A. Monoclonal antibodies to nucleic acid-containing cellular constituents: probes for molecular biology and autoimmune disease. Proc. Natl. Acad. Sci. USA78, 2737–2741 (1981). ArticleCAS Google Scholar